|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-380 |
0e+00 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 559.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 1 MEIYADYAATTPVKPEVVDAMMTIYNSHYGNPSSIHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKG 80
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 IVKANEQLGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYD 160
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 161 IQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDyPQL-GGEQELKRRAGTENL 239
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLE-PLIhGGGQERGLRSGTENV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 240 AQIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQERAIPFELNGSMTDATGHIVNLYFPFVEVETMLTLLDMAQIYVS 319
Cdd:COG1104 241 PGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446331312 320 SGSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
3-380 |
1.15e-149 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 427.80 E-value: 1.15e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPSSIHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIV 82
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 83 KANEQlGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYDIQ 162
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 163 DIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDyPQL-GGEQELKRRAGTENLAQ 241
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFR-PLLrGGHQERGRRAGTENVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 242 IVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQERaIPF-ELNGSMTDATGHIVNLYFPFVEVETMLTLLDMAQIYVSS 320
Cdd:TIGR03402 239 IVGLGKAAELATEHLEEENTRVRALRDRLEAGLLAR-IPDaRLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 321 GSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:TIGR03402 318 GSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMS 377
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
3-380 |
7.17e-129 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 375.82 E-value: 7.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMM---TIyNSHYGNPSS-IHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAI 78
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMpylTM-DGTFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 79 KGIVKANEQLGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQI 158
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 159 YDIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLV--KDHVTLDYPQLGGEQELKRRAGT 236
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVrrKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 237 ENLAQIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQEraipFE---LNGSMTDATGHIVNLYFPFVEVET-MLTLLD 312
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKD----IEevyLNGDLEQRVPGNLNVSFNYVEGESlIMALKD 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446331312 313 MAqiyVSSGSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:PRK14012 320 LA---VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELS 384
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
3-364 |
4.55e-82 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 254.86 E-value: 4.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNP-SSIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNTAIKG 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 iVKANEQLGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIY 159
Cdd:pfam00266 81 -LGRSLKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 160 DIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDH--VTLDYPQLGG----------- 226
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDllEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 227 ---EQELKRRAGTENLAQIVGMAKALQ-LAEKNRDDNNIHLMNLKEQFLVKLQEraIP-FELNGSmtDATGHIVNLYFPF 301
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLS--LPgIRLYGP--ERRASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446331312 302 VEVETMLTLLDMAQIYVSSGSACtagsTQPSHVLDAMfedeersNHSIRFSFNELTTENEINA 364
Cdd:pfam00266 316 VHPHDVATLLDESGIAVRSGHHC----AQPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
3-369 |
1.82e-60 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 199.23 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPS-SIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNTAIKG 80
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 IVKANEQlGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIY 159
Cdd:cd06453 81 LGRANKP-GDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 160 DIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDYP--QLGGE---------- 227
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPpyGGGGEmieevsfeet 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 228 --QELKRR--AGTENLAQIVGMAKALQLAEKnRDDNNI--HLMNLKEQFLVKLqeRAIP-FELNGSMTDATGhIVNLYFP 300
Cdd:cd06453 240 tyADLPHKfeAGTPNIAGAIGLGAAIDYLEK-IGMEAIaaHEHELTAYALERL--SEIPgVRVYGDAEDRAG-VVSFNLE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446331312 301 FVEVETMLTLLDMAQIYVSSGSACtagsTQPSHvlDAMFEdeersNHSIRFSFNELTTENEINAIVAEI 369
Cdd:cd06453 316 GIHPHDVATILDQYGIAVRAGHHC----AQPLM--RRLGV-----PGTVRASFGLYNTEEEIDALVEAL 373
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-249 |
2.08e-18 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 6 DYAATTPvKPEVV-DAMMTIYNSHygNpSSIH-------AKGRDArkYlDESRRQIAQLLGA-DTHEIIFTSGATESNNT 76
Cdd:NF041166 250 DNAATTQ-KPQAViDRLSYFYEHE--N-SNIHraahelaARATDA--Y-EGAREKVRRFIGApSVDEIIFVRGTTEAINL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 77 AIKGIVKANEQLGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTV 155
Cdd:NF041166 323 VAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLaQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 156 QQiydIQDIIAETNAY---FHVDAVQAIGHL--DVKfdefEIDA----MSitAHKFGGPKGVGALLVKDHVTLDYP--QL 224
Cdd:NF041166 403 TP---VKEIIALAHRAgakVLVDGAQSVSHMpvDVQ----ALDAdffvFS--GHKVFGPTGIGVVYGKRDLLEAMPpwQG 473
|
250 260 270
....*....|....*....|....*....|....*....
gi 446331312 225 GG--------EQEL------KRRAGTENLAQIVGMAKAL 249
Cdd:NF041166 474 GGnmiadvtfEKTVyqpapnRFEAGTGNIADAVGLGAAL 512
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| NifS |
COG1104 |
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino ... |
1-380 |
0e+00 |
|
Cysteine desulfurase/Cysteine sulfinate desulfinase IscS or related enzyme, NifS family [Amino acid transport and metabolism];
Pssm-ID: 440721 [Multi-domain] Cd Length: 381 Bit Score: 559.67 E-value: 0e+00
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 1 MEIYADYAATTPVKPEVVDAMMTIYNSHYGNPSSIHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKG 80
Cdd:COG1104 2 MMIYLDNAATTPVDPEVLEAMLPYLTEYFGNPSSLHSFGREARAALEEAREQVAALLGADPEEIIFTSGGTEANNLAIKG 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 IVKANEQLGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYD 160
Cdd:COG1104 82 AARAYRKKGKHIITSAIEHPAVLETARFLEKEGFEVTYLPVDEDGRVDLEALEAALRPDTALVSVMHANNETGTIQPIAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 161 IQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDyPQL-GGEQELKRRAGTENL 239
Cdd:COG1104 162 IAEIAKEHGVLFHTDAVQAVGKIPVDVKELGVDLLSLSAHKIYGPKGVGALYVRKGVRLE-PLIhGGGQERGLRSGTENV 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 240 AQIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQERAIPFELNGSMTDATGHIVNLYFPFVEVETMLTLLDMAQIYVS 319
Cdd:COG1104 241 PGIVGLGKAAELAAEELEEEAARLRALRDRLEEGLLAAIPGVVINGDPENRLPNTLNFSFPGVEGEALLLALDLAGIAVS 320
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446331312 320 SGSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:COG1104 321 SGSACSSGSLEPSHVLLAMGLDEELAHGSIRFSLGRFTTEEEIDRAIEALKEIVARLRKLS 381
|
|
| FeS_nifS |
TIGR03402 |
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related ... |
3-380 |
1.15e-149 |
|
cysteine desulfurase NifS; Members of this protein family are NifS, one of several related families of cysteine desulfurase involved in iron-sulfur (FeS) cluster biosynthesis. NifS is part of the NIF system, usually associated with other nif genes involved in nitrogenase expression and nitrogen fixation. The protein family is given a fairly broad interpretation here. It includes a clade nearly always found in extended nitrogen fixation genomic regions, plus a second clade more closely related to the first than to IscS and also part of NifS-like/NifU-like systems. This model does not extend to a more distantly clade found in the epsilon proteobacteria such as Helicobacter pylori, also named NifS in the literature, built instead in TIGR03403.
Pssm-ID: 132443 [Multi-domain] Cd Length: 379 Bit Score: 427.80 E-value: 1.15e-149
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPSSIHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIV 82
Cdd:TIGR03402 1 IYLDNNATTRVDPEVLEAMLPYFTEYFGNPSSMHSFGGEVGKAVEEAREQVAKLLGAEPDEIIFTSGGTESDNTAIKSAL 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 83 KANEQlGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYDIQ 162
Cdd:TIGR03402 81 AAQPE-KRHIITTAVEHPAVLSLCQHLEKQGYKVTYLPVDEEGRLDLEELRAAITDDTALVSVMWANNETGTIFPIEEIG 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 163 DIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDyPQL-GGEQELKRRAGTENLAQ 241
Cdd:TIGR03402 160 EIAKERGALFHTDAVQAVGKIPIDLKEMNIDMLSLSGHKLHGPKGVGALYIRKGTRFR-PLLrGGHQERGRRAGTENVPG 238
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 242 IVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQERaIPF-ELNGSMTDATGHIVNLYFPFVEVETMLTLLDMAQIYVSS 320
Cdd:TIGR03402 239 IVGLGKAAELATEHLEEENTRVRALRDRLEAGLLAR-IPDaRLNGDPTKRLPNTVNISFEYIEGEAILLLLDMEGICASS 317
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 321 GSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:TIGR03402 318 GSACTSGSLEPSHVLRAMGVPHTAAHGSIRFSLSRYNTEEDIDYVLEVLPPIIARLRAMS 377
|
|
| PRK14012 |
PRK14012 |
IscS subfamily cysteine desulfurase; |
3-380 |
7.17e-129 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 184450 [Multi-domain] Cd Length: 404 Bit Score: 375.82 E-value: 7.17e-129
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMM---TIyNSHYGNPSS-IHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAI 78
Cdd:PRK14012 5 IYLDYSATTPVDPRVAEKMMpylTM-DGTFGNPASrSHRFGWQAEEAVDIARNQIADLIGADPREIVFTSGATESDNLAI 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 79 KGIVKANEQLGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQI 158
Cdd:PRK14012 84 KGAAHFYQKKGKHIITSKTEHKAVLDTCRQLEREGFEVTYLDPQSNGIIDLEKLEAAMRDDTILVSIMHVNNEIGVIQDI 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 159 YDIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLV--KDHVTLDYPQLGGEQELKRRAGT 236
Cdd:PRK14012 164 AAIGEICRERGIIFHVDAAQSVGKVPIDLSKLKVDLMSFSAHKIYGPKGIGALYVrrKPRVRLEAQMHGGGHERGMRSGT 243
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 237 ENLAQIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQEraipFE---LNGSMTDATGHIVNLYFPFVEVET-MLTLLD 312
Cdd:PRK14012 244 LPTHQIVGMGEAARIAKEEMATENERIRALRDRLWNGIKD----IEevyLNGDLEQRVPGNLNVSFNYVEGESlIMALKD 319
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 446331312 313 MAqiyVSSGSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:PRK14012 320 LA---VSSGSACTSASLEPSYVLRALGLNDELAHSSIRFSLGRFTTEEEIDYAIELVRKSIGKLRELS 384
|
|
| PLN02651 |
PLN02651 |
cysteine desulfurase |
3-362 |
7.87e-124 |
|
cysteine desulfurase
Pssm-ID: 178257 [Multi-domain] Cd Length: 364 Bit Score: 361.66 E-value: 7.87e-124
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPSSI-HAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGI 81
Cdd:PLN02651 1 LYLDMQATTPIDPRVLDAMLPFLIEHFGNPHSRtHLYGWESEDAVEKARAQVAALIGADPKEIIFTSGATESNNLAIKGV 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 82 VKANEQLGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYDI 161
Cdd:PLN02651 81 MHFYKDKKKHVITTQTEHKCVLDSCRHLQQEGFEVTYLPVKSDGLVDLDELAAAIRPDTALVSVMAVNNEIGVIQPVEEI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 162 QDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVK--DHVTLDYPQLGGEQELKRRAGTENL 239
Cdd:PLN02651 161 GELCREKKVLFHTDAAQAVGKIPVDVDDLGVDLMSISGHKIYGPKGVGALYVRrrPRVRLEPLMSGGGQERGRRSGTENT 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 240 AQIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQERAIPFELNGSMTDATGHI--VNLYFPFVEVETML-TLLDMAqi 316
Cdd:PLN02651 241 PLVVGLGAACELAMKEMDYDEKHMKALRERLLNGLRAKLGGVRVNGPRDPEKRYPgtLNLSFAYVEGESLLmGLKEVA-- 318
|
330 340 350 360
....*....|....*....|....*....|....*....|....*.
gi 446331312 317 yVSSGSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEI 362
Cdd:PLN02651 319 -VSSGSACTSASLEPSYVLRALGVPEEMAHGSLRLGVGRFTTEEEV 363
|
|
| DNA_S_dndA |
TIGR03235 |
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a ... |
4-352 |
1.56e-120 |
|
cysteine desulfurase DndA; This model describes DndA, a protein related to IscS and part of a larger family of cysteine desulfurases. It is encoded, typically, divergently from a conserved, sparsely distributed operon for sulfur modification of DNA. This modification system is designated dnd, after the phenotype of DNA degradation during electrophoresis. The system is sporadically distributed in bacteria, much like some restriction enzyme operons. DndB is described as a putative ATPase. [DNA metabolism, Restriction/modification]
Pssm-ID: 163191 [Multi-domain] Cd Length: 353 Bit Score: 352.95 E-value: 1.56e-120
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 4 YADYAATTPVKPEVVDAMMTIYNSHYGNPSSI-HAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIV 82
Cdd:TIGR03235 1 YLDHNATTPIDPAVAEAMLPWLLEEFGNPSSRtHEFGHNAKKAVERARKQVAEALGADTEEVIFTSGATESNNLAILGLA 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 83 KANEQLG-NHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYDI 161
Cdd:TIGR03235 81 RAGEQKGkKHIITSAIEHPAVLEPIRALERNGFTVTYLPVDESGRIDVDELADAIRPDTLLVSIMHVNNETGSIQPIREI 160
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 162 QDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDYP----QLGGEQELKRRAGTE 237
Cdd:TIGR03235 161 AEVLEAHEAFFHVDAAQVVGKITVDLSADRIDLISCSGHKIYGPKGIGALVIRKRGKPKAPlkpiMFGGGQERGLRPGTL 240
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 238 NLAQIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQerAIPFELNGSMTDATGHIVNLYFPFVEVETMLTLLdMAQIY 317
Cdd:TIGR03235 241 PVHLIVGMGEAAEIARRNAQAWEVKLRAMRNQLRDALQ--TLGVKLNGDPAETIPHILNFSIDGVNSEALIVNL-RADAA 317
|
330 340 350
....*....|....*....|....*....|....*
gi 446331312 318 VSSGSACTAGSTQPSHVLDAMFEDEERSNHSIRFS 352
Cdd:TIGR03235 318 VSTGSACSSSKYEPSHVLQAMGLDTDRARGAIRFS 352
|
|
| PRK02948 |
PRK02948 |
IscS subfamily cysteine desulfurase; |
3-380 |
2.13e-97 |
|
IscS subfamily cysteine desulfurase;
Pssm-ID: 179511 [Multi-domain] Cd Length: 381 Bit Score: 294.71 E-value: 2.13e-97
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPSSIHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIV 82
Cdd:PRK02948 2 IYLDYAATTPMSKEALQTYQKAASQYFGNESSLHDIGGTASSLLQVCRKTFAEMIGGEEQGIYFTSGGTESNYLAIQSLL 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 83 KANEQLGNHIITSKIEHHSVLHVFEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYDIQ 162
Cdd:PRK02948 82 NALPQNKKHIITTPMEHASIHSYFQSLESQGYTVTEIPVDKSGLIRLVDLERAITPDTVLASIQHANSEIGTIQPIAEIG 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 163 DIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLD--YPqlGGEQELKRRAGTENLA 240
Cdd:PRK02948 162 ALLKKYNVLFHSDCVQTFGKLPIDVFEMGIDSLSVSAHKIYGPKGVGAVYINPQVRWKpvFP--GTTHEKGFRPGTVNVP 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 241 QIVGMAKALQLAEKNRDDNNIHLMNLKEQFLVKLQERAIPFELNGSMTDATGHIVNLYFPFVEVE-TMLTlLDMAQIYVS 319
Cdd:PRK02948 240 GIAAFLTAAENILKNMQEESLRFKELRSYFLEQIQTLPLPIEVEGHSTSCLPHIIGVTIKGIEGQyTMLE-CNRRGIAIS 318
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446331312 320 SGSACTAGSTQPSHVLDAMFEDEERSNHSIRFSFNELTTENEINAIVAEIHKIYFKFKEES 380
Cdd:PRK02948 319 TGSACQVGKQEPSKTMLAIGKTYEEAKQFVRFSFGQQTTKDQIDTTIHALETIGNQFYRGV 379
|
|
| Aminotran_5 |
pfam00266 |
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes ... |
3-364 |
4.55e-82 |
|
Aminotransferase class-V; This domain is found in amino transferases, and other enzymes including cysteine desulphurase EC:4.4.1.-.
Pssm-ID: 425567 [Multi-domain] Cd Length: 368 Bit Score: 254.86 E-value: 4.55e-82
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNP-SSIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNTAIKG 80
Cdd:pfam00266 1 IYLDSAATTQKPQEVLDAIQEYYTDYNGNVhRGVHTLGKEATQAYEEAREKVAEFINApSNDEIIFTSGTTEAINLVALS 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 iVKANEQLGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIY 159
Cdd:pfam00266 81 -LGRSLKPGDEIVITEMEHHANLVPWQELaKRTGARVRVLPLDEDGLLDLDELEKLITPKTKLVAITHVSNVTGTIQPVP 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 160 DIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDH--VTLDYPQLGG----------- 226
Cdd:pfam00266 160 EIGKLAHQYGALVLVDAAQAIGHRPIDVQKLGVDFLAFSGHKLYGPTGIGVLYGRRDllEKMPPLLGGGgmietvslqes 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 227 ---EQELKRRAGTENLAQIVGMAKALQ-LAEKNRDDNNIHLMNLKEQFLVKLQEraIP-FELNGSmtDATGHIVNLYFPF 301
Cdd:pfam00266 240 tfaDAPWKFEAGTPNIAGIIGLGAALEyLSEIGLEAIEKHEHELAQYLYERLLS--LPgIRLYGP--ERRASIISFNFKG 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446331312 302 VEVETMLTLLDMAQIYVSSGSACtagsTQPSHVLDAMfedeersNHSIRFSFNELTTENEINA 364
Cdd:pfam00266 316 VHPHDVATLLDESGIAVRSGHHC----AQPLMVRLGL-------GGTVRASFYIYNTQEDVDR 367
|
|
| CsdA |
COG0520 |
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism]; |
3-372 |
2.85e-69 |
|
Selenocysteine lyase/Cysteine desulfurase [Amino acid transport and metabolism];
Pssm-ID: 440286 [Multi-domain] Cd Length: 396 Bit Score: 222.71 E-value: 2.85e-69
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPvKPE-VVDAMMTIYNSHYGNPS-SIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNTAIK 79
Cdd:COG0520 17 VYLDNAATGQ-KPRpVIDAIRDYYEPYNANVHrGAHELSAEATDAYEAAREKVARFIGAaSPDEIIFTRGTTEAINLVAY 95
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 80 GIVKANEqlGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQI 158
Cdd:COG0520 96 GLGRLKP--GDEILITEMEHHSNIVPWQELaERTGAEVRVIPLDEDGELDLEALEALLTPRTKLVAVTHVSNVTGTVNPV 173
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 159 YDIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHV--TLDYPQLGGE--------- 227
Cdd:COG0520 174 KEIAALAHAHGALVLVDGAQSVPHLPVDVQALGCDFYAFSGHKLYGPTGIGVLYGKRELleALPPFLGGGGmiewvsfdg 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 228 ---QELKRR--AGTENLAQIVGMAKALQLAEK-NRDDNNIHLMNLKEQFLVKLQEraIP-FELNGSMTDAT-GHIVNLYF 299
Cdd:COG0520 254 ttyADLPRRfeAGTPNIAGAIGLGAAIDYLEAiGMEAIEARERELTAYALEGLAA--IPgVRILGPADPEDrSGIVSFNV 331
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 446331312 300 PFVEVETMLTLLDMAQIYVSSGSACtagsTQPSHvldamfeDEERSNHSIRFSFNELTTENEINAIVAEIHKI 372
Cdd:COG0520 332 DGVHPHDVAALLDDEGIAVRAGHHC----AQPLM-------RRLGVPGTVRASFHLYNTEEEIDRLVEALKKL 393
|
|
| SufS_like |
cd06453 |
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP) ... |
3-369 |
1.82e-60 |
|
Cysteine desulfurase (SufS)-like. This family belongs to the pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to cysteine desulfurase (SufS) and selenocysteine lyase. SufS catalyzes the removal of elemental sulfur and selenium atoms from L-cysteine, L-cystine, L-selenocysteine, and L-selenocystine to produce L-alanine; and selenocysteine lyase catalyzes the decomposition of L-selenocysteine.
Pssm-ID: 99746 [Multi-domain] Cd Length: 373 Bit Score: 199.23 E-value: 1.82e-60
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPS-SIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNTAIKG 80
Cdd:cd06453 1 VYLDNAATSQKPQPVIDAIVDYYRHYNANVHrGVHELSARATDAYEAAREKVARFINApSPDEIIFTRNTTEAINLVAYG 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 IVKANEQlGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIY 159
Cdd:cd06453 81 LGRANKP-GDEIVTSVMEHHSNIVPWQQLaERTGAKLKVVPVDDDGQLDLEALEKLLTERTKLVAVTHVSNVLGTINPVK 159
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 160 DIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDYP--QLGGE---------- 227
Cdd:cd06453 160 EIGEIAHEAGVPVLVDGAQSAGHMPVDVQDLGCDFLAFSGHKMLGPTGIGVLYGKEELLEEMPpyGGGGEmieevsfeet 239
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 228 --QELKRR--AGTENLAQIVGMAKALQLAEKnRDDNNI--HLMNLKEQFLVKLqeRAIP-FELNGSMTDATGhIVNLYFP 300
Cdd:cd06453 240 tyADLPHKfeAGTPNIAGAIGLGAAIDYLEK-IGMEAIaaHEHELTAYALERL--SEIPgVRVYGDAEDRAG-VVSFNLE 315
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 446331312 301 FVEVETMLTLLDMAQIYVSSGSACtagsTQPSHvlDAMFEdeersNHSIRFSFNELTTENEINAIVAEI 369
Cdd:cd06453 316 GIHPHDVATILDQYGIAVRAGHHC----AQPLM--RRLGV-----PGTVRASFGLYNTEEEIDALVEAL 373
|
|
| PLN02855 |
PLN02855 |
Bifunctional selenocysteine lyase/cysteine desulfurase |
3-249 |
2.41e-29 |
|
Bifunctional selenocysteine lyase/cysteine desulfurase
Pssm-ID: 215460 [Multi-domain] Cd Length: 424 Bit Score: 117.54 E-value: 2.41e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIY-----NSHYGnpssIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNT 76
Cdd:PLN02855 34 VYLDNAATSQKPAAVLDALQDYYeeynsNVHRG----IHALSAKATDAYELARKKVAAFINAsTSREIVFTRNATEAINL 109
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 77 AIKGIVKANEQLGNHIITSKIEHHSVLhVFEQL--EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGT 154
Cdd:PLN02855 110 VAYTWGLANLKPGDEVILSVAEHHSNI-VPWQLvaQKTGAVLKFVGLTPDEVLDVEQLKELLSEKTKLVATHHVSNVLGS 188
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 155 VQQIYDIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKDHVTLDYPQL--GGE----- 227
Cdd:PLN02855 189 ILPVEDIVHWAHAVGAKVLVDACQSVPHMPVDVQTLGADFLVASSHKMCGPTGIGFLWGKSDLLESMPPFlgGGEmisdv 268
|
250 260 270
....*....|....*....|....*....|.
gi 446331312 228 -------QELKRR--AGTENLAQIVGMAKAL 249
Cdd:PLN02855 269 fldhstyAPPPSRfeAGTPAIGEAIGLGAAI 299
|
|
| PRK10874 |
PRK10874 |
cysteine desulfurase CsdA; |
3-371 |
7.96e-29 |
|
cysteine desulfurase CsdA;
Pssm-ID: 182799 [Multi-domain] Cd Length: 401 Bit Score: 115.91 E-value: 7.96e-29
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTpVKPE-VVDAMMTIYNSHYGN-PSSIHAKGRDARKYLDESRRQIAQLLGA-DTHEIIFTSGATESNNTAIK 79
Cdd:PRK10874 21 VYLDSAATA-LKPQaVIEATQQFYSLSAGNvHRSQFAAAQRLTARYEAAREQVAQLLNApDAKNIVWTRGTTESINLVAQ 99
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 80 GIVKANEQLGNHIITSKIEHHS----VLHVFEQLereGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTV 155
Cdd:PRK10874 100 SYARPRLQPGDEIIVSEAEHHAnlvpWLMVAQQT---GAKVVKLPLGADRLPDVDLLPELITPRTRILALGQMSNVTGGC 176
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 156 QqiyDIQDIIA---ETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVK-DHVTLDYPQLGG----- 226
Cdd:PRK10874 177 P---DLARAITlahQAGMVVMVDGAQGAVHFPADVQALDIDFYAFSGHKLYGPTGIGVLYGKsELLEAMSPWQGGgkmlt 253
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 227 --------EQELKRR--AGTENLAQIVGMAKALQ-LAEKNRDDNNIH---LMNLKEQFLVKLqERAIPFELNGSMTdatg 292
Cdd:PRK10874 254 evsfdgftPQSAPWRfeAGTPNVAGVIGLSAALEwLADIDINQAESWsrsLATLAEDALAKL-PGFRSFRCQDSSL---- 328
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 293 hivnLYFPFVEV--ETMLTLLDMAQIYVSSGSACtagsTQPshVLDAMfedeeRSNHSIRFSFNELTTENEINAIVAEIH 370
Cdd:PRK10874 329 ----LAFDFAGVhhSDLVTLLAEYGIALRAGQHC----AQP--LLAAL-----GVTGTLRASFAPYNTQSDVDALVNAVD 393
|
.
gi 446331312 371 K 371
Cdd:PRK10874 394 R 394
|
|
| PRK09295 |
PRK09295 |
cysteine desulfurase SufS; |
3-249 |
2.17e-23 |
|
cysteine desulfurase SufS;
Pssm-ID: 181766 [Multi-domain] Cd Length: 406 Bit Score: 100.60 E-value: 2.17e-23
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGN-PSSIHAKGRDARKYLDESRRQIAQLLGADTHE-IIFTSGATESNNTAIKG 80
Cdd:PRK09295 25 AYLDSAASAQKPSQVIDAEAEFYRHGYAAvHRGIHTLSAQATEKMENVRKQAALFINARSAEeLVFVRGTTEGINLVANS 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 81 IVKANEQLGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIY 159
Cdd:PRK09295 105 WGNSNVRAGDNIIISEMEHHANIVPWQMLcARVGAELRVIPLNPDGTLQLETLPALFDERTRLLAITHVSNVLGTENPLA 184
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 160 DIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKGVGALLVKD-----------------HVTLDYP 222
Cdd:PRK09295 185 EMIALAHQHGAKVLVDGAQAVMHHPVDVQALDCDFYVFSGHKLYGPTGIGILYVKEallqemppwegggsmiaTVSLTEG 264
|
250 260
....*....|....*....|....*..
gi 446331312 223 QLGGEQELKRRAGTENLAQIVGMAKAL 249
Cdd:PRK09295 265 TTWAKAPWRFEAGTPNTGGIIGLGAAL 291
|
|
| am_tr_V_VC1184 |
TIGR01976 |
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of ... |
3-277 |
4.04e-22 |
|
cysteine desulfurase family protein, VC1184 subfamily; This model describes a subfamily of probable pyridoxal phosphate-dependent enzymes in the aminotransferase class V family (pfam00266). The most closely related characterized proteins are active as cysteine desulfurases, selenocysteine lyases, or both; some are involved in FeS cofactor biosynthesis and are designated NifS. An active site Cys residue present in those sequences, in motifs resembling GHHC or GSAC, is not found in this family. The function of members of this family is unknown, but seems unlike to be as an aminotransferase. [Unknown function, Enzymes of unknown specificity]
Pssm-ID: 273906 [Multi-domain] Cd Length: 397 Bit Score: 96.75 E-value: 4.04e-22
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 3 IYADYAATTPVKPEVVDAMMTIYNSHYGNPSSIHAKGRDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIV 82
Cdd:TIGR01976 19 VFFDNPAGTQIPQSVADAVSAALTRSNANRGGAYESSRRADQVVDDAREAVADLLNADPPEVVFGANATSLTFLLSRAIS 98
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 83 KaNEQLGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVD-DTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYD 160
Cdd:TIGR01976 99 R-RWGPGDEVIVTRLDHEANISPWLQAaERAGAKVKWARVDeATGELHPDDLASLLSPRTRLVAVTAASNTLGSIVDLAA 177
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 161 IQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHKFGGPKgVGALLVKDHV-------TLDYPQLGGEQELKrr 233
Cdd:TIGR01976 178 ITELVHAAGALVVVDAVHYAPHGLIDVQATGADFLTCSAYKFFGPH-MGILWGRPELlmnlppyKLTFSYDTGPERFE-- 254
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 446331312 234 AGT---ENLAqivGMAKALQ-LAEKNRDDNNI--------------HLMNLKEQFLVKLQER 277
Cdd:TIGR01976 255 LGTpqyELLA---GVVAAVDyLAGLGESANGSrrerlvasfqaidaYENRLAEYLLVGLSDL 313
|
|
| f2_encap_cargo1 |
NF041166 |
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like ... |
6-249 |
2.08e-18 |
|
family 2A encapsulin nanocompartment cargo protein cysteine desulfurase; Capsid-like encapsulin nanocompartments are commonly found in bacteria and archaea. Encapsulin nanocompartments, which are assembled from shell proteins, encapsulate various cargo proteins, typically peroxidases or ferritin-like proteins, to protect cells from oxidative stress caused by peroxide. Proteins of this family are cysteine desulfurases with an additional N-terminal encapsulation targeting sequence (~200 aa) that is necessary and sufficient for compartmentalization.
Pssm-ID: 469077 [Multi-domain] Cd Length: 623 Bit Score: 86.83 E-value: 2.08e-18
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 6 DYAATTPvKPEVV-DAMMTIYNSHygNpSSIH-------AKGRDArkYlDESRRQIAQLLGA-DTHEIIFTSGATESNNT 76
Cdd:NF041166 250 DNAATTQ-KPQAViDRLSYFYEHE--N-SNIHraahelaARATDA--Y-EGAREKVRRFIGApSVDEIIFVRGTTEAINL 322
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 77 AIKGIVKANEQLGNHIITSKIEHHSVLHVFEQL-EREGFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTV 155
Cdd:NF041166 323 VAKSWGRQNIGAGDEIIVSHLEHHANIVPWQQLaQETGAKLRVIPVDDSGQILLDEYAKLLNPRTKLVSVTQVSNALGTV 402
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 156 QQiydIQDIIAETNAY---FHVDAVQAIGHL--DVKfdefEIDA----MSitAHKFGGPKGVGALLVKDHVTLDYP--QL 224
Cdd:NF041166 403 TP---VKEIIALAHRAgakVLVDGAQSVSHMpvDVQ----ALDAdffvFS--GHKVFGPTGIGVVYGKRDLLEAMPpwQG 473
|
250 260 270
....*....|....*....|....*....|....*....
gi 446331312 225 GG--------EQEL------KRRAGTENLAQIVGMAKAL 249
Cdd:NF041166 474 GGnmiadvtfEKTVyqpapnRFEAGTGNIADAVGLGAAL 512
|
|
| GadA |
COG0076 |
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport ... |
7-265 |
1.73e-16 |
|
Glutamate or tyrosine decarboxylase or a related PLP-dependent protein [Amino acid transport and metabolism]; Glutamate or tyrosine decarboxylase or a related PLP-dependent protein is part of the Pathway/BioSystem: Pantothenate/CoA biosynthesis
Pssm-ID: 439846 [Multi-domain] Cd Length: 460 Bit Score: 80.65 E-value: 1.73e-16
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 7 YAATTPVkPEVVDAMMTIYNSHYGN----PSSIHAkgrdarkyldESR--RQIAQLLGADTHEI-IFTSGATESN----- 74
Cdd:COG0076 75 TGGTTPA-ALAADLLASALNQNMGDwdtsPAATEL----------EREvvRWLADLLGLPEGAGgVFTSGGTEANllall 143
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 75 ---NTAIKGIVKANEQLGNH---IITSKIEHHSV---LHVFEqLEREGfdVTYLDVDDTGAIDLDQLEETITD------K 139
Cdd:COG0076 144 aarDRALARRVRAEGLPGAPrprIVVSEEAHSSVdkaARLLG-LGRDA--LRKVPVDEDGRMDPDALEAAIDEdraaglN 220
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 140 TILVsimfvnneVGTVQQ----IYD----IQDIIAETNAYFHVDAvqAIG-------HLDVKFDEFEiDAMSIT--AHKF 202
Cdd:COG0076 221 PIAV--------VATAGTtntgAIDplaeIADIAREHGLWLHVDA--AYGgfalpspELRHLLDGIE-RADSITvdPHKW 289
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 203 GG-PKGVGALLVKD--------HVTLDY-PQLGGEQ--------ELKRRA------------GTENLAQIV--GMAKALQ 250
Cdd:COG0076 290 LYvPYGCGAVLVRDpellreafSFHASYlGPADDGVpnlgdytlELSRRFralklwatlralGREGYRELIerCIDLARY 369
|
330
....*....|....*
gi 446331312 251 LAEKNRDDNNIHLMN 265
Cdd:COG0076 370 LAEGIAALPGFELLA 384
|
|
| AAT_I |
cd01494 |
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP) ... |
46-214 |
6.71e-15 |
|
Aspartate aminotransferase (AAT) superfamily (fold type I) of pyridoxal phosphate (PLP)-dependent enzymes. PLP combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. Structure and sequence analysis has revealed that the PLP dependent enzymes can be classified into four major groups of different evolutionary origin: aspartate aminotransferase superfamily (fold type I), tryptophan synthase beta superfamily (fold type II), alanine racemase superfamily (fold type III), and D-amino acid superfamily (fold type IV) and Glycogen phophorylase family (fold type V).
Pssm-ID: 99742 [Multi-domain] Cd Length: 170 Bit Score: 72.03 E-value: 6.71e-15
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 46 LDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIVKAneqlGNHIITSKIEHHSVLHVFEqlEREGFDVTYLDVDDTG 125
Cdd:cd01494 2 LEELEEKLARLLQPGNDKAVFVPSGTGANEAALLALLGP----GDEVIVDANGHGSRYWVAA--ELAGAKPVPVPVDDAG 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 126 A--IDLDQLEET-ITDKTILVSIMFVNNEVGTVQQIYDIQDIIAETNAYFHVDAVQAIGHLDVKF---DEFEIDAMSITA 199
Cdd:cd01494 76 YggLDVAILEELkAKPNVALIVITPNTTSGGVLVPLKEIRKIAKEYGILLLVDAASAGGASPAPGvliPEGGADVVTFSL 155
|
170
....*....|....*
gi 446331312 200 HKFGGPKGVGALLVK 214
Cdd:cd01494 156 HKNLGGEGGGVVIVK 170
|
|
| PucG |
COG0075 |
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism ... |
11-215 |
3.03e-12 |
|
Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG [Amino acid transport and metabolism, Nucleotide transport and metabolism]; Archaeal aspartate aminotransferase or a related aminotransferase, includes purine catabolism protein PucG is part of the Pathway/BioSystem: Serine biosynthesis
Pssm-ID: 439845 [Multi-domain] Cd Length: 376 Bit Score: 67.04 E-value: 3.03e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 11 TPVKPEVVDAMMTIYNSHYGNpssihakgrDARKYLDESRRQIAQLLGADTHEIIFTSGATESNNTAIKGIVKANEqlgn 90
Cdd:COG0075 9 TPVPPRVLRAMARPMIGHRDP---------EFVELMDEVRELLKKVFGTENDVVILTGSGTGAMEAALANLVSPGD---- 75
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 91 hiitskiehhSVLHV----F-----EQLEREGFDVTYLDVDDTGAIDLDQLEETI-TDKTILVsIMFVNNEV--GTVQQI 158
Cdd:COG0075 76 ----------KVLVLvngaFgerwaEIAERYGAEVVVLEVPWGEAVDPEEVEEALaADPDIKA-VAVVHNETstGVLNPL 144
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|....*...
gi 446331312 159 YDIQDIIAETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHK-FGGPKGVGALLVKD 215
Cdd:COG0075 145 EEIGALAKEHGALLIVDAVSSLGGVPLDMDEWGIDVVVSGSQKcLMLPPGLAFVAVSE 202
|
|
| DOPA_deC_like |
cd06450 |
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
11-265 |
1.46e-11 |
|
DOPA decarboxylase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to DOPA/tyrosine decarboxylase (DDC), histidine decarboxylase (HDC), and glutamate decarboxylase (GDC). DDC is active as a dimer and catalyzes the decarboxylation of tyrosine. GDC catalyzes the decarboxylation of glutamate and HDC catalyzes the decarboxylation of histidine.
Pssm-ID: 99743 [Multi-domain] Cd Length: 345 Bit Score: 64.92 E-value: 1.46e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 11 TPVKPEVVDAMMTIY--NSHYGNPSSIHAkgrdARKYLDESRRQIAQLLGADTHEI--IFTSGATESNNTAI-------K 79
Cdd:cd06450 7 TTMDPPALLLEMLTSakNAIDFTWDESPA----ATEMEAEVVNWLAKLFGLPSEDAdgVFTSGGSESNLLALlaardraR 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 80 GIVKANEQLGNH---IITSKIEHHSV---LHVFEQleregfDVTYLDVDDTGAIDLDQLEETITD------KTILVSIMF 147
Cdd:cd06450 83 KRLKAGGGRGIDklvIVCSDQAHVSVekaAAYLDV------KVRLVPVDEDGRMDPEALEAAIDEdkaeglNPIMVVATA 156
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 148 VNNEVGTVQQIYDIQDIIAETNAYFHVDAvqAIGHLDVKFDEFE-ID-----AMSITA--HKFGG-PKGVGALLVKdhvt 218
Cdd:cd06450 157 GTTDTGAIDPLEEIADLAEKYDLWLHVDA--AYGGFLLPFPEPRhLDfgierVDSISVdpHKYGLvPLGCSAVLVR---- 230
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....
gi 446331312 219 ldypqlggeqELK-----RRAGTENLAQIV--GMAKALQLAEKNRDDNNIHLMN 265
Cdd:cd06450 231 ----------ALKlwatlRRFGRDGYGEHIdrIVDLAKYLAELIRADPGFELLG 274
|
|
| AGAT_like |
cd06451 |
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate ... |
11-213 |
4.96e-10 |
|
Alanine-glyoxylate aminotransferase (AGAT) family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). The major groups in this CD correspond to alanine-glyoxylate aminotransferase (AGAT), serine-glyoxylate aminotransferase (SGAT), and 3-hydroxykynurenine transaminase (HKT). AGAT is a homodimeric protein, which catalyses the transamination of glyoxylate to glycine, and SGAT converts serine and glyoxylate to hydroxypyruvate and glycine. HKT catalyzes the PLP-dependent transamination of 3-hydroxykynurenine, a potentially toxic metabolite of the kynurenine pathway.
Pssm-ID: 99744 [Multi-domain] Cd Length: 356 Bit Score: 60.38 E-value: 4.96e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 11 TPVKPEVVDAMmtiynshyGNP--SSIHAKGRDARKYLDESRRQIAQLLGADTheIIFTSGATESNNTAIKGIVKAneql 88
Cdd:cd06451 8 SNVPPRVLKAM--------NRPmlGHRSPEFLALMDEILEGLRYVFQTENGLT--FLLSGSGTGAMEAALSNLLEP---- 73
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 89 GNHIITSKIEHHSVLHVfEQLEREGFDVTYLDVDDTGAIDLDQLEETITDKTIlVSIMFVNNE--VGTVQQIYDIQDIIA 166
Cdd:cd06451 74 GDKVLVGVNGVFGDRWA-DMAERYGADVDVVEKPWGEAVSPEEIAEALEQHDI-KAVTLTHNEtsTGVLNPLEGIGALAK 151
|
170 180 190 200
....*....|....*....|....*....|....*....|....*...
gi 446331312 167 ETNAYFHVDAVQAIGHLDVKFDEFEIDAMSITAHK-FGGPKGVGALLV 213
Cdd:cd06451 152 KHDALLIVDAVSSLGGEPFRMDEWGVDVAYTGSQKaLGAPPGLGPIAF 199
|
|
| PLN02409 |
PLN02409 |
serine--glyoxylate aminotransaminase |
89-209 |
2.19e-07 |
|
serine--glyoxylate aminotransaminase
Pssm-ID: 178031 [Multi-domain] Cd Length: 401 Bit Score: 52.45 E-value: 2.19e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 89 GNHIITSKIEHHSVLhVFEQLEREGFDVTYLDVDDTGAIDLDQLEETI---TDKTILVsIMFVNNE--VGTVQQIYDIQD 163
Cdd:PLN02409 84 GDKVVSFRIGQFSLL-WIDQMQRLNFDVDVVESPWGQGADLDILKSKLrqdTNHKIKA-VCVVHNEtsTGVTNDLAGVRK 161
|
90 100 110 120
....*....|....*....|....*....|....*....|....*....
gi 446331312 164 II--AETNAYFHVDAVQAIGHLDVKFDEFEID-AMSITAHKFGGPKGVG 209
Cdd:PLN02409 162 LLdcAQHPALLLVDGVSSIGALDFRMDEWGVDvALTGSQKALSLPTGLG 210
|
|
| PRK07324 |
PRK07324 |
transaminase; Validated |
47-177 |
8.15e-06 |
|
transaminase; Validated
Pssm-ID: 235989 Cd Length: 373 Bit Score: 47.24 E-value: 8.15e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 47 DESRRQIAQLL-GADTHEIIFTSGATESNNTAIKGIVKAneqlGNHIItskiehhSVLHVFEQL----EREGFDVTYLDV 121
Cdd:PRK07324 65 PEFKEAVASLYqNVKPENILQTNGATGANFLVLYALVEP----GDHVI-------SVYPTYQQLydipESLGAEVDYWQL 133
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|.
gi 446331312 122 DDTGAI--DLDQLEETITDKTILVSIMFVNNEVGTVQQ---IYDIQDIIAETNAYFHVDAV 177
Cdd:PRK07324 134 KEENGWlpDLDELRRLVRPNTKLICINNANNPTGALMDrayLEEIVEIARSVDAYVLSDEV 194
|
|
| AAT_like |
cd00609 |
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent ... |
6-177 |
1.20e-04 |
|
Aspartate aminotransferase family. This family belongs to pyridoxal phosphate (PLP)-dependent aspartate aminotransferase superfamily (fold I). Pyridoxal phosphate combines with an alpha-amino acid to form a compound called a Schiff base or aldimine intermediate, which depending on the reaction, is the substrate in four kinds of reactions (1) transamination (movement of amino groups), (2) racemization (redistribution of enantiomers), (3) decarboxylation (removing COOH groups), and (4) various side-chain reactions depending on the enzyme involved. Pyridoxal phosphate (PLP) dependent enzymes were previously classified into alpha, beta and gamma classes, based on the chemical characteristics (carbon atom involved) of the reaction they catalyzed. The availability of several structures allowed a comprehensive analysis of the evolutionary classification of PLP dependent enzymes, and it was found that the functional classification did not always agree with the evolutionary history of these enzymes. The major groups in this CD corresponds to Aspartate aminotransferase a, b and c, Tyrosine, Alanine, Aromatic-amino-acid, Glutamine phenylpyruvate, 1-Aminocyclopropane-1-carboxylate synthase, Histidinol-phosphate, gene products of malY and cobC, Valine-pyruvate aminotransferase and Rhizopine catabolism regulatory protein.
Pssm-ID: 99734 [Multi-domain] Cd Length: 350 Bit Score: 43.48 E-value: 1.20e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 6 DYAATTPVKPEVVDAMMTIYNSHYGNPSSIhakgrdarkylDESRRQIAQLLG------ADTHEIIFTSGATESNNTAIK 79
Cdd:cd00609 9 DFPPPPEVLEALAAAALRAGLLGYYPDPGL-----------PELREAIAEWLGrrggvdVPPEEIVVTNGAQEALSLLLR 77
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 80 GIVKAneqlGNHIITSKIEHHSVLHVFEQLEREgFDVTYLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTV---Q 156
Cdd:cd00609 78 ALLNP----GDEVLVPDPTYPGYEAAARLAGAE-VVPVPLDEEGGFLLDLELLEAAKTPKTKLLYLNNPNNPTGAVlseE 152
|
170 180
....*....|....*....|.
gi 446331312 157 QIYDIQDIIAETNAYFHVDAV 177
Cdd:cd00609 153 ELEELAELAKKHGILIISDEA 173
|
|
| tyr_nico_aTase |
TIGR01265 |
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal ... |
12-166 |
2.05e-04 |
|
tyrosine/nicotianamine family aminotransferase; This subfamily of pyridoxal phosphate-dependent enzymes includes known examples of both tyrosine aminotransferase from animals and nicotianamine aminotransferase from barley.
Pssm-ID: 188123 Cd Length: 403 Bit Score: 43.10 E-value: 2.05e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 12 PVKPEVVDAMMTIYNSHYGN---PSSIHAKGRDA-RKYLdesRRQIAQLLGADthEIIFTSGATESNNTAIKGIVKAneq 87
Cdd:TIGR01265 48 RTDPEAEEAVKDALRSGKFNgyaPSVGALAAREAvAEYL---SSDLPGKLTAD--DVVLTSGCSQAIEICIEALANP--- 119
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 88 lGNHIITSK--IEHHSVLHVFEQLEREGFDvtyLDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTVQQIYDIQDII 165
Cdd:TIGR01265 120 -GANILVPRpgFPLYDTRAAFSGLEVRLYD---LLPEKDWEIDLDGLESLADEKTVAIVVINPSNPCGSVFSRDHLQKIA 195
|
.
gi 446331312 166 A 166
Cdd:TIGR01265 196 E 196
|
|
| Aminotran_1_2 |
pfam00155 |
Aminotransferase class I and II; |
36-175 |
5.85e-04 |
|
Aminotransferase class I and II;
Pssm-ID: 395103 [Multi-domain] Cd Length: 351 Bit Score: 41.52 E-value: 5.85e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 36 HAKGRDARKYLD-----ESRRQIAQLLGADT-------HEIIFTSGATESNNTAIkgIVKANEqlGNHIITSKIEHHSVL 103
Cdd:pfam00155 26 ALAGGTRNLYGPtdghpELREALAKFLGRSPvlkldreAAVVFGSGAGANIEALI--FLLANP--GDAILVPAPTYASYI 101
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 446331312 104 HVFEqleREGFDVTY--LDVDDTGAIDLDQLEETITDKTILVSIMFVNNEVGTV---QQIYDIQDIIAETNAYFHVD 175
Cdd:pfam00155 102 RIAR---LAGGEVVRypLYDSNDFHLDFDALEAALKEKPKVVLHTSPHNPTGTVatlEELEKLLDLAKEHNILLLVD 175
|
|
| GDC-P |
cd00613 |
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine ... |
109-216 |
6.67e-03 |
|
Glycine cleavage system P-protein, alpha- and beta-subunits. This family consists of Glycine cleavage system P-proteins EC:1.4.4.2 from bacterial, mammalian and plant sources. The P protein is part of the glycine decarboxylase multienzyme complex EC:2.1.2.10 (GDC) also annotated as glycine cleavage system or glycine synthase. GDC consists of four proteins P, H, L and T. The reaction catalysed by this protein is: Glycine + lipoylprotein <=> S-aminomethyldihydrolipoylprotein + CO2. Alpha-beta-type dimers associate to form an alpha(2)beta(2) tetramer, where the alpha- and beta-subunits are structurally similar and appear to have arisen by gene duplication and subsequent divergence with a loss of one active site. The members of this CD are widely dispersed among all three forms of cellular life.
Pssm-ID: 99737 [Multi-domain] Cd Length: 398 Bit Score: 38.37 E-value: 6.67e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 446331312 109 LEREGFDVTYLDVDDTGAIDLDQLEETITDKTilVSIMFVN-NEVGTV-QQIYDIQDIIAETNAYFHVDA-------VQA 179
Cdd:cd00613 129 GEPLGIEVVEVPSDEGGTVDLEALKEEVSEEV--AALMVQYpNTLGVFeDLIKEIADIAHSAGALVYVDGdnlnltgLKP 206
|
90 100 110 120
....*....|....*....|....*....|....*....|...
gi 446331312 180 IGhldvkfdEFEIDAMSITAHKF------GGPkGVGALLVKDH 216
Cdd:cd00613 207 PG-------EYGADIVVGNLQKTgvphggGGP-GAGFFAVKKE 241
|
|
| |
